메뉴 건너뛰기




Volumn 10, Issue 4, 2000, Pages 267-278

Executionary pathway for apoptosis: Lessons from mutant mice

Author keywords

Apoptosis; Caspases; Death receptors; Mitochondria; Progammed cell death

Indexed keywords

CAENORHABDITIS ELEGANS; MAMMALIA;

EID: 0034569527     PISSN: 10010602     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cr.7290054     Document Type: Review
Times cited : (39)

References (68)
  • 1
  • 2
    • 0022497852 scopus 로고
    • Genetic control of programmed cell death in the nematode C. elegans
    • Ellis HM, Horvitz HR. Genetic control of programmed cell death in the nematode C. elegans. Cell 1986; 44:817-29.
    • (1986) Cell , vol.44 , pp. 817-829
    • Ellis, H.M.1    Horvitz, H.R.2
  • 3
    • 0033593572 scopus 로고    scopus 로고
    • Cell death in development
    • Vaux DL, Korsmeyer SJ. Cell death in development. Cell 1999; 96:245-54.
    • (1999) Cell , vol.96 , pp. 245-254
    • Vaux, D.L.1    Korsmeyer, S.J.2
  • 4
    • 0025255636 scopus 로고
    • The Caenorhabditis elegans genes ced-3 and ced-4 act cell autonomously to cause programmed cell death
    • Yuan JY, Horvitz HR. The Caenorhabditis elegans genes ced-3 and ced-4 act cell autonomously to cause programmed cell death. Dev Biol 1990; 138:33-41.
    • (1990) Dev Biol , vol.138 , pp. 33-41
    • Yuan, J.Y.1    Horvitz, H.R.2
  • 5
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 β-converting enzume
    • Yuan J, Shaham S, Ledoux S, Ellis HM, Horvitz HR. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 β-converting enzume. Cell 1993; 75:641-52.
    • (1993) Cell , vol.75 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5
  • 6
    • 0034105784 scopus 로고    scopus 로고
    • Apaf-1 oligomerized into biologically active approximately 700-kDa and inactive approximately 1.4-MDa apoptosome complexes
    • Cain K, Bratton SB, Langlais C et al. Apaf-1 oligomerized into biologically active approximately 700-kDa and inactive approximately 1.4-MDa apoptosome complexes. J Biol Chem 2000; 275:6067-70.
    • (2000) J Biol Chem , vol.275 , pp. 6067-6070
    • Cain, K.1    Bratton, S.B.2    Langlais, C.3
  • 7
    • 0032524885 scopus 로고    scopus 로고
    • The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9
    • Conradt B, Horvitz HR. The C. elegans protein EGL-1 is required for programmed cell death and interacts with the Bcl-2-like protein CED-9. Cell 1998; 93:519-29.
    • (1998) Cell , vol.93 , pp. 519-529
    • Conradt, B.1    Horvitz, H.R.2
  • 8
    • 0032509238 scopus 로고    scopus 로고
    • Caenorhabditis elegans EGL-1 disrupts the interaction of CED-9 with CED-4 and promotes CED-3 activation
    • del Peso L, Gonzalez VM, Nunez G. Caenorhabditis elegans EGL-1 disrupts the interaction of CED-9 with CED-4 and promotes CED-3 activation. J Biol Chem 1998; 273:33495-500.
    • (1998) J Biol Chem , vol.273 , pp. 33495-33500
    • Del Peso, L.1    Gonzalez, V.M.2    Nunez, G.3
  • 9
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H, Henzel WJ, Liu X, Lutschg A, Wang X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3 [see comments]. Cell 1997; 90:405-13.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 10
    • 0033532091 scopus 로고    scopus 로고
    • Human CARD4 protein is a novel CED-4/Apaf-1 cell death family member that activates NF-κB
    • Bertin J, Nir WJ, Fischer CM et al. Human CARD4 protein is a novel CED-4/Apaf-1 cell death family member that activates NF-κB. J Biol Chem 1999; 274:12955-8.
    • (1999) J Biol Chem , vol.274 , pp. 12955-12958
    • Bertin, J.1    Nir, W.J.2    Fischer, C.M.3
  • 11
    • 0033591330 scopus 로고    scopus 로고
    • Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-κB
    • Inohara N, Koseki T, del Peso L et al. Nod1, an Apaf-1-like activator of caspase-9 and nuclear factor-κB. J Biol Chem 1999; 274:14560-7.
    • (1999) J Biol Chem , vol.274 , pp. 14560-14567
    • Inohara, N.1    Koseki, T.2    Del Peso, L.3
  • 12
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams JM, Cory S. The Bcl-2 protein family: arbiters of cell survival. Science 1998; 281:1322-6.
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 13
    • 0032409781 scopus 로고    scopus 로고
    • Bcl-2 family proeins
    • Reed JC. Bcl-2 family proeins. Oncogene 1998; 17:3225-36.
    • (1998) Oncogene , vol.17 , pp. 3225-3236
    • Reed, J.C.1
  • 14
    • 12944270500 scopus 로고    scopus 로고
    • An apoptosis regulator at the intersection of caspases and Bcl-2 family proteins
    • Zhang H, Xu Q, Krajewski S et al. An apoptosis regulator at the intersection of caspases and Bcl-2 family proteins. Proc Natl Acad Sci USA 2000; 97:2597-602.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2597-2602
    • Zhang, H.1    Xu, Q.2    Krajewski, S.3
  • 15
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry Na, Lazebnik Y. Caspases: enemies within. Science 1998; 281:1312-6.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, Na.1    Lazebnik, Y.2
  • 18
    • 0032910169 scopus 로고    scopus 로고
    • Apoptosis control by death and decoy receptors
    • Ashkenazi A, Dixit VM. Apoptosis control by death and decoy receptors. Curr Opin Cell Biol 1999; 11:255-60.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 255-260
    • Ashkenazi, A.1    Dixit, V.M.2
  • 19
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 1996; 86:147-57.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 20
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin SA, Lorenzo HK, Zamzami N et al. Molecular characterization of mitochondrial apoptosis-inducing factor [see comments]. Nature 1999; 397:441-6.
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1    Lorenzo, H.K.2    Zamzami, N.3
  • 21
    • 0034117177 scopus 로고    scopus 로고
    • Mitochondrio-nuclear translocation of AIF in apoptosis and necrosis
    • Daugas E, Susin SA, Zamzami N et al. Mitochondrio-nuclear translocation of AIF in apoptosis and necrosis. Faseb J 2000; 14:729-39.
    • (2000) Faseb J , vol.14 , pp. 729-739
    • Daugas, E.1    Susin, S.A.2    Zamzami, N.3
  • 22
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen AM, Ekert PG, Pakusch M et al. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 2000; 102:43-53.
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3
  • 23
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C, Fang M, Li Y, Li L, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000; 102:33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 24
    • 0028913550 scopus 로고
    • A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain
    • Boldin MP, Varfolomeev EE, Pancer Z, Mett IL, Camonis JH, Wallach D. A novel protein that interacts with the death domain of Fas/APO1 contains a sequence motif related to the death domain. J Biol Chem 1995; 270:7795-8.
    • (1995) J Biol Chem , vol.270 , pp. 7795-7798
    • Boldin, M.P.1    Varfolomeev, E.E.2    Pancer, Z.3    Mett, I.L.4    Camonis, J.H.5    Wallach, D.6
  • 25
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan AM, O'Rourke K, Tewari M, Dixit VM. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 1995; 81:505-12.
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 26
    • 0034733584 scopus 로고    scopus 로고
    • Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations
    • Siegel RM, Frederiksen JK, Zacharias DA et al. Fas preassociation required for apoptosis signaling and dominant inhibition by pathogenic mutations [see comments]. Science 2000; 288:2354-7.
    • (2000) Science , vol.288 , pp. 2354-2357
    • Siegel, R.M.1    Frederiksen, J.K.2    Zacharias, D.A.3
  • 27
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/ FADD-interacting protease, in Fas/APO1- and TNF receptor-induced cell death
    • Boldin M P, Goncharov TM, Goltsev YV, Wallach D. Involvement of MACH, a novel MORT1/ FADD-interacting protease, in Fas/APO1- and TNF receptor-induced cell death. Cell 1996; 85:803-15.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 28
    • 15844412409 scopus 로고    scopus 로고
    • FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex
    • Muzio M, Chinnaiyan AM, Kischkel FC et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 1996; 85:817-27.
    • (1996) Cell , vol.85 , pp. 817-827
    • Muzio, M.1    Chinnaiyan, A.M.2    Kischkel, F.C.3
  • 29
    • 0028883850 scopus 로고
    • Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. An induced proximity model for caspase-8 activation
    • Kischkel FC, Hellbardt S, Behrmann I et al. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. An induced proximity model for caspase-8 activation. Embo J 1995; 14:5579-88.
    • (1995) Embo J , vol.14 , pp. 5579-5588
    • Kischkel, F.C.1    Hellbardt, S.2    Behrmann, I.3
  • 31
    • 0029978182 scopus 로고    scopus 로고
    • Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis
    • Enari M, Talanian RV, Wong WW, Nagata S. Sequential activation of ICE-like and CPP32-like proteases during Fas-mediated apoptosis. Nature 1996; 380:723-6.
    • (1996) Nature , vol.380 , pp. 723-726
    • Enari, M.1    Talanian, R.V.2    Wong, W.W.3    Nagata, S.4
  • 32
    • 8544225061 scopus 로고    scopus 로고
    • Affnity labeling displays the stepwise activation of ICE-related proteases by Fas, staurosporine, and CrmA-sensitive caspase-8
    • Takahashi A, Hirata H, Yonehara S et al. Affnity labeling displays the stepwise activation of ICE-related proteases by Fas, staurosporine, and CrmA-sensitive caspase-8. Oncogene 1997; 14:2741-52.
    • (1997) Oncogene , vol.14 , pp. 2741-2752
    • Takahashi, A.1    Hirata, H.2    Yonehara, S.3
  • 33
    • 0029025549 scopus 로고
    • Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family
    • Fernandes-Alnemri T, Litwack G, Alnemri ES. Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family. Cancer Res 1995; 55:2737-42.
    • (1995) Cancer Res , vol.55 , pp. 2737-2742
    • Fernandes-Alnemri, T.1    Litwack, G.2    Alnemri, E.S.3
  • 34
    • 0033179212 scopus 로고    scopus 로고
    • An exegesis of IAPs: Salvation and surprises from BIR motifs
    • Miller LK. An exegesis of IAPs: salvation and surprises from BIR motifs. Trends Cell Biol 1999; 9:323-8.
    • (1999) Trends Cell Biol , vol.9 , pp. 323-328
    • Miller, L.K.1
  • 35
    • 0034607655 scopus 로고    scopus 로고
    • Ubiquitin protein ligase activity of IAPs and their degradation in in protesomes in response to apoptotic stimuli
    • Yang Y, Fang S, Jensen JP, Weissman AM, Ashwell JD. Ubiquitin protein ligase activity of IAPs and their degradation in in protesomes in response to apoptotic stimuli. Science 2000; 288:874-7.
    • (2000) Science , vol.288 , pp. 874-877
    • Yang, Y.1    Fang, S.2    Jensen, J.P.3    Weissman, A.M.4    Ashwell, J.D.5
  • 38
    • 0032575723 scopus 로고    scopus 로고
    • Essential role of CED-4 oligomerization in CED-3 activation and apoptosis
    • Yang X, Chang HY, Baltimore D. Essential role of CED-4 oligomerization in CED-3 activation and apoptosis [see comments]. Science 1998; 281:1355-7.
    • (1998) Science , vol.281 , pp. 1355-1357
    • Yang, X.1    Chang, H.Y.2    Baltimore, D.3
  • 39
    • 0342978014 scopus 로고    scopus 로고
    • Cell-specific induction of apoptosis by microinjection of cytochrome c. Bcl-xL has activity independent c of cytochrome c release
    • Li F, Srinivasan A, Wang Y, Armstrong RC, Tomaselli KJ, Fritz LC. Cell-specific induction of apoptosis by microinjection of cytochrome c. Bcl-xL has activity independent c of cytochrome c release. J Biol Chem 1997; 272:30299-305.
    • (1997) J Biol Chem , vol.272 , pp. 30299-30305
    • Li, F.1    Srinivasan, A.2    Wang, Y.3    Armstrong, R.C.4    Tomaselli, K.J.5    Fritz, L.C.6
  • 40
    • 0032576692 scopus 로고    scopus 로고
    • Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c
    • Rosse T, Olivier R, Monney L et al. Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c [see comments]. Nature 1998; 391:496-9.
    • (1998) Nature , vol.391 , pp. 496-499
    • Rosse, T.1    Olivier, R.2    Monney, L.3
  • 42
    • 0034641980 scopus 로고    scopus 로고
    • Apoptosis in development
    • Meier P, Finch A, Evan G. Apoptosis in development [In Process Citation]. Nature 2000; 407:796-801.
    • (2000) Nature , vol.407 , pp. 796-801
    • Meier, P.1    Finch, A.2    Evan, G.3
  • 43
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • Nagata S. Apoptosis by death factor. Cell 1997; 88:355-65.
    • (1997) Cell , vol.88 , pp. 355-365
    • Nagata, S.1
  • 44
    • 0031080895 scopus 로고    scopus 로고
    • Cellular environments and apoptosis: Tissue microenvironments control activated T-cell death
    • Akbar AN, Salmon M. Cellular environments and apoptosis: tissue microenvironments control activated T-cell death. Immunol Today 1997; 18:72-6.
    • (1997) Immunol Today , vol.18 , pp. 72-76
    • Akbar, A.N.1    Salmon, M.2
  • 45
    • 7144263731 scopus 로고    scopus 로고
    • FADD: Essential for embryo development and signaling from some, but not all, inducers of apoptosis
    • Yeh WC, Pompa JL, McCurrach ME et al. FADD: essential for embryo development and signaling from some, but not all, inducers of apoptosis. Science 1998; 279:1954-8.
    • (1998) Science , vol.279 , pp. 1954-1958
    • Yeh, W.C.1    Pompa, J.L.2    McCurrach, M.E.3
  • 46
    • 0032143986 scopus 로고    scopus 로고
    • Targeted disruption of the mouse Caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apol, and DR3 and is lethal prenatally
    • Varfolomeev EE, Schuchmann M, Luria V et al. Targeted disruption of the mouse Caspase 8 gene ablates cell death induction by the TNF receptors, Fas/Apol, and DR3 and is lethal prenatally. Immunity 1998; 9:267-76.
    • (1998) Immunity , vol.9 , pp. 267-276
    • Varfolomeev, E.E.1    Schuchmann, M.2    Luria, V.3
  • 47
    • 0033662341 scopus 로고    scopus 로고
    • Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development
    • Yeh WC, Itie A, Elia AJ et al. Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development [In Process Citation]. Immunity 2000; 12:633-42.
    • (2000) Immunity , vol.12 , pp. 633-642
    • Yeh, W.C.1    Itie, A.2    Elia, A.J.3
  • 48
    • 0029956641 scopus 로고    scopus 로고
    • Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice
    • Kuida K, Zheng TS, Na S et al. Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature 1996; 384:368-72.
    • (1996) Nature , vol.384 , pp. 368-372
    • Kuida, K.1    Zheng, T.S.2    Na, S.3
  • 49
    • 15644364847 scopus 로고    scopus 로고
    • Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes
    • Woo M, Hakem R, Soengas MS et al. Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes. Genes Dev 1998; 12:806-19.
    • (1998) Genes Dev , vol.12 , pp. 806-819
    • Woo, M.1    Hakem, R.2    Soengas, M.S.3
  • 50
    • 0032514713 scopus 로고    scopus 로고
    • Resistamce to DNA fragmentation and chromatin condensation in mice lacking the DNA fragmentation factor 45
    • Zhang J, Liu X, Scherer DC, van Kaer L, Wang X, Xu M. Resistamce to DNA fragmentation and chromatin condensation in mice lacking the DNA fragmentation factor 45. Proc Natl Acad Sci USA 1998; 95:12480-5.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12480-12485
    • Zhang, J.1    Liu, X.2    Scherer, D.C.3    Van Kaer, L.4    Wang, X.5    Xu, M.6
  • 51
    • 0032736175 scopus 로고    scopus 로고
    • In vivo evidence that caspase-3 is required for Fas-mediated apoptosis of hepatocytes
    • Woo M, Hakem A, Elia AJ et al. In vivo evidence that caspase-3 is required for Fas-mediated apoptosis of hepatocytes. J Immunol 1999; 163:4909-16.
    • (1999) J Immunol , vol.163 , pp. 4909-4916
    • Woo, M.1    Hakem, A.2    Elia, A.J.3
  • 52
    • 0032493910 scopus 로고    scopus 로고
    • Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9
    • Kuida K, Haydar TF, Kuan CY et al. Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9. Cell 1998; 94:325-37.
    • (1998) Cell , vol.94 , pp. 325-337
    • Kuida, K.1    Haydar, T.F.2    Kuan, C.Y.3
  • 53
    • 0032493870 scopus 로고    scopus 로고
    • Differential requirement for caspase 9 in apoptotic pathways in vivo
    • Hakem R, Hakem A, Duncan GS et al. Differential requirement for caspase 9 in apoptotic pathways in vivo. Cell 1998; 94:339-52.
    • (1998) Cell , vol.94 , pp. 339-352
    • Hakem, R.1    Hakem, A.2    Duncan, G.S.3
  • 54
    • 0032544564 scopus 로고    scopus 로고
    • Apaf1 is rwquired for mitochondrial pathways of apoptosis and brain development
    • Yoshida H, Kong YY, Yoshida R et al. Apaf1 is rwquired for mitochondrial pathways of apoptosis and brain development. Cell 1998; 94:739-50.
    • (1998) Cell , vol.94 , pp. 739-750
    • Yoshida, H.1    Kong, Y.Y.2    Yoshida, R.3
  • 55
    • 0032544449 scopus 로고    scopus 로고
    • Apaf1 (CED-4 homolog) regulates programmed cell deathin mammalian development
    • Cecconi F, Alvarez-Bolado G, Meyer BI, Roth KA, Gruss P. Apaf1 (CED-4 homolog) regulates programmed cell deathin mammalian development. Cell 1998; 94:727-37.
    • (1998) Cell , vol.94 , pp. 727-737
    • Cecconi, F.1    Alvarez-Bolado, G.2    Meyer, B.I.3    Roth, K.A.4    Gruss, P.5
  • 56
    • 0034640102 scopus 로고    scopus 로고
    • Cytochrome c deficiency causes embryonic lethality and attenuates stress-induced apoptosis
    • Li K, Li Y, Shelton JM et al. Cytochrome c deficiency causes embryonic lethality and attenuates stress-induced apoptosis. Cell 2000; 101:389-99.
    • (2000) Cell , vol.101 , pp. 389-399
    • Li, K.1    Li, Y.2    Shelton, J.M.3
  • 57
    • 0032080197 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • Bergeron L, Perez GI, Macdonald G et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β. Genes Dev 1998; 12:1304-14.
    • (1998) Genes Dev , vol.12 , pp. 1304-1314
    • Bergeron, L.1    Perez, G.I.2    Macdonald, G.3
  • 58
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA, Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β. Nature 2000; 403:676:5-103.
    • (2000) Nature , vol.403 , pp. 6765-7103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 59
    • 0032536771 scopus 로고    scopus 로고
    • Two CD95 (APO-1/Fas) signaling pathways
    • Scaffidi C, Fulda S, Srinivasan A et al. Two CD95 (APO-1/Fas) signaling pathways. Embo J 1998; 17:1675-87.
    • (1998) Embo J , vol.17 , pp. 1675-1687
    • Scaffidi, C.1    Fulda, S.2    Srinivasan, A.3
  • 60
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X, Budihardjo I, Zou H, Slaughter C, Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998; 94:481-90.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 61
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 1998; 94:491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 62
    • 0033534446 scopus 로고    scopus 로고
    • L prevents this release but not tumor necrosis factor-R1/Fas death
    • L prevents this release but not tumor necrosis factor-R1/Fas death. J Biol Chem 1999; 274:1156-63.
    • (1999) J Biol Chem , vol.274 , pp. 1156-1163
    • Gross, A.1    Yin, X.M.2    Wang, K.3
  • 63
    • 0033607006 scopus 로고    scopus 로고
    • Bid-deficient mice are resistant to Fas-inducde hepatocellular apoptosis
    • Yin XM, Wang K, Gross A et al. Bid-deficient mice are resistant to Fas-inducde hepatocellular apoptosis. Nature 1999; 400:886-91.
    • (1999) Nature , vol.400 , pp. 886-891
    • Yin, X.M.1    Wang, K.2    Gross, A.3
  • 64
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane
    • Eskes R, Desagher S, Antonsson B, Martinou JC. Bid induces the oligomerization and insertion of Bax into the outer mitochondrial membrane. Mol Cell Biol 2000; 20:929-35.
    • (2000) Mol Cell Biol , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 65
    • 0034663829 scopus 로고    scopus 로고
    • tBid, a membrane-targeted death ligand, oligomerized BAK to release cytochrome c
    • Wei MC, Lindsten T, Mootha VK et al. tBid, a membrane-targeted death ligand, oligomerized BAK to release cytochrome c. Genes Dev 2000; 14:2060-71.
    • (2000) Genes Dev , vol.14 , pp. 2060-2071
    • Wei, M.C.1    Lindsten, T.2    Mootha, V.K.3
  • 66
    • 0033378016 scopus 로고    scopus 로고
    • Early activation of caspases during T lymphocyte stimulation results in selective substrate cleavage in nonapoptotic cells
    • Alam A, Cohen LY, Aouad S, Sekaly RP. Early activation of caspases during T lymphocyte stimulation results in selective substrate cleavage in nonapoptotic cells. J Exp Med 1999; 190:1879-90.
    • (1999) J Exp Med , vol.190 , pp. 1879-1890
    • Alam, A.1    Cohen, L.Y.2    Aouad, S.3    Sekaly, R.P.4
  • 67
    • 0033386808 scopus 로고    scopus 로고
    • Caspase activation is required for T cell proliferation
    • Kennedy N J, Kataoka T, Tschopp J, Budd RC. Caspase activation is required for T cell proliferation. J Exp Med 1999; 190:1891-6.
    • (1999) J Exp Med , vol.190 , pp. 1891-1896
    • Kennedy, N.J.1    Kataoka, T.2    Tschopp, J.3    Budd, R.C.4
  • 68
    • 0032549670 scopus 로고    scopus 로고
    • Caspase-dependent cleavage of signaling proteins during apoptosis. A turn-off mechanism for anti-apoptotic signals
    • Widmann C, Gibson S, Johnson GL. Caspase-dependent cleavage of signaling proteins during apoptosis. A turn-off mechanism for anti-apoptotic signals. J Biol Chem 1998; 273:7141-7.
    • (1998) J Biol Chem , vol.273 , pp. 7141-7147
    • Widmann, C.1    Gibson, S.2    Johnson, G.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.